The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
The mitochondrial permeability transition pore: a mystery solved?
Open accessAbstract
The permeability transition (PT) denotes an increase of the mitochondrial inner membrane permeability to solutes with molecular masses up to about 1500 Da. It is presumed to be mediated by opening of a channel, the permeability transition pore (PTP), whose molecular nature remains a mystery. Here I briefly review the history of the PTP, discuss existing models, and present our new results indicating that reconstituted dimers of the FOF1 ATP synthase form a channel with properties identical to those of the mitochondrial megachannel (MMC), the electrophysiological equivalent of the PTP. Open questions remain, but there is now promise that the PTP can be studied by genetic methods to solve the large number of outstanding problems.
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Cites
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“CyPD is the mitochondrial receptor for CsA and modulates the PTP but is not a structural pore component (Baines et al., 2005; Basso et al., 2005; Nakagawa et al., 2005; Schinzel et al., 2005).”
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“CyPD is the mitochondrial receptor for CsA and modulates the PTP but is not a structural pore component (Baines et al., 2005; Basso et al., 2005; Nakagawa et al., 2005; Schinzel et al., 2005).”
BackgroundSelf-citationp53 Opens the Mitochondrial Permeability Transition Pore to Trigger Necrosis
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Cited by
Activation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731
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Szeto, H. H. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12461 · Cited by 548
Mitochondria, Bioenergetics and Apoptosis in Cancer
Burke, P. J. (2017) · Trends in Cancer · doi:10.1016/j.trecan.2017.10.006 · Cited by 432
Mitochondria in innate immune signaling
Banoth, B., & Cassel, S. L. (2018) · Translational Research · doi:10.1016/j.trsl.2018.07.014 · Cited by 410
Metadata
- Authors
- Bernardi, P.
- Venue
- Frontiers in Physiology
- Publisher
- Frontiers Media SA
- Published
- 2013
- Volume
- 4
- Pages
- 95-95
- ISSN
- 1664-042X (ISSN-L)
- OpenAlex
- W2030618370
- Cited by
- 335
- References
- 18
- FWCI
- 22.59
- Type
- journal article
- Language
- en
- Open access
- gold
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
